1h3e: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1h3e.gif|left|200px]] | [[Image:1h3e.gif|left|200px]] | ||
'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND TYROSINOL''' | {{Structure | ||
|PDB= 1h3e |SIZE=350|CAPTION= <scene name='initialview01'>1h3e</scene>, resolution 2.90Å | |||
|SITE= <scene name='pdbsite=AC1:Tyb+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=TYB:TYROSINAL'>TYB</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] | |||
|GENE= | |||
}} | |||
'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND TYROSINOL''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1H3E is a [ | 1H3E is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3E OCA]. | ||
==Reference== | ==Reference== | ||
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition., Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S, EMBO J. 2002 Jul 15;21(14):3829-40. PMID:[http:// | Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition., Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S, EMBO J. 2002 Jul 15;21(14):3829-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12110594 12110594] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
| Line 22: | Line 31: | ||
[[Category: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]] | [[Category: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:31:37 2008'' | ||
Revision as of 09:31, 20 March 2008
| |||||||||||||
| 1h3e, resolution 2.90Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1 | ||||||||||||
| Ligands: | ATP and TYB | ||||||||||||
| Activity: | Tyrosine--tRNA ligase, with EC number 6.1.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND TYROSINOL
Overview
Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked C-terminal domain of approximately 80 residues, which has hitherto been disordered in crystal structures of the enzyme. We have determined the structure of Thermus thermophilus TyrRS at 2.0 A resolution in a crystal form in which the C-terminal domain is ordered, and confirm that the fold is similar to part of the C-terminal domain of ribosomal protein S4. We have also determined the structure at 2.9 A resolution of the complex of T.thermophilus TyrRS with cognate tRNA(tyr)(G Psi A). In this structure, the C-terminal domain binds between the characteristic long variable arm of the tRNA and the anti-codon stem, thus recognizing the unique shape of the tRNA. The anticodon bases have a novel conformation with A-36 stacked on G-34, and both G-34 and Psi-35 are base-specifically recognized. The tRNA binds across the two subunits of the dimeric enzyme and, remarkably, the mode of recognition of the class I TyrRS for its cognate tRNA resembles that of a class II synthetase in being from the major groove side of the acceptor stem.
About this Structure
1H3E is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition., Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S, EMBO J. 2002 Jul 15;21(14):3829-40. PMID:12110594 [[Category: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]]
Page seeded by OCA on Thu Mar 20 11:31:37 2008